Journal article
Use of yeast as a system to study amyloid toxicity
Methods (San Diego, Calif.), Vol.53(3), pp.226-231
03/2011
DOI: 10.1016/j.ymeth.2010.11.007
PMCID: PMC3432305
PMID: 21115125
Abstract
The formation of amyloid-like fibrils is a hallmark of several neurodegenerative diseases. How the assembly of amyloid-like fibrils contributes to cell death is a major unresolved question in the field. The budding yeast Saccharomyces cerevisiae is a powerful model organism to study basic mechanisms for how cellular pathways regulate amyloid assembly and proteotoxicity. For example, studies of the amyloidogenic yeast prion [RNQ(+)] have revealed novel roles by which molecular chaperones protect cells from the accumulation of cytotoxic protein species. In budding yeast there are a variety of cellular assays that can be employed to analyze the assembly of amyloid-like aggregates and mechanistically dissect how cellular pathways influence proteotoxicity. In this review, we describe several assays that are routinely used to investigate aggregation and toxicity of the [RNQ(+)] prion in yeast.
Details
- Title: Subtitle
- Use of yeast as a system to study amyloid toxicity
- Creators
- Daniel W Summers - Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, 526 Taylor Hall CB# 7090, Chapel Hill, NC 27514, USA. daniel_summers@med.unc.eduDouglas M Cyr
- Resource Type
- Journal article
- Publication Details
- Methods (San Diego, Calif.), Vol.53(3), pp.226-231
- Publisher
- United States
- DOI
- 10.1016/j.ymeth.2010.11.007
- PMID
- 21115125
- PMCID
- PMC3432305
- ISSN
- 1046-2023
- eISSN
- 1095-9130
- Grant note
- 5F31AG032790 / NIA NIH HHS\nR01 GM067785 / NIGMS NIH HHS\n5R01GM067785 / NIGMS NIH HHS\nF31 AG032790 / NIA NIH HHS\nR01 GM056981 / NIGMS NIH HHS
- Language
- English
- Date published
- 03/2011
- Academic Unit
- Iowa Neuroscience Institute; Biology
- Record Identifier
- 9984070114502771
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